Hemoglobin Release

Hemoglobin release is the liberation of hemoglobin from red blood cells, an important event in blood analysis, cell biology, and biological sample preparation. It occurs when the erythrocyte membrane is disrupted, often by osmotic imbalance that drives water into the cell and causes hemolysis, or by mechanical and chemical lysis methods. The released hemoglobin can then be quantified spectrophotometrically, separated for biochemical analysis, or used to assess membrane stability and hemolytic effects. Controlled hemoglobin release supports studies of erythrocyte physiology, blood-material interactions, diagnostic testing, and the evaluation of drugs or conditions that damage red blood cells.

Hemoglobin Release - Related Videos

Research

JoVE EoE - Neuropathology

Modeling Neonatal Intraventricular Hemorrhage Through Intraventricular Injection of Hemoglobin

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2025

This video demonstrates a method to generate a rat model of neonatal intraventricular hemorrhage. In this procedure, an anesthetized rat pup is injected with hemoglobin into the lateral ventricle of the brain. The hemoglobin causes oxidative stress and releases heme, simulating intraventricular hemorrhage. The resulting damage to brain tissues, driven by reactive oxygen species and inflammatory cytokines, leads to ventricular enlargement, a common consequence of intraventricular hemorrhage.

Modeling Neonatal Intraventricular Hemorrhage Through Intraventricular Injection of Hemoglobin

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Cited by 12 •

2022

We present a model of neonatal intraventricular hemorrhage using rat pups that mimics the pathology seen in humans.

Education

JoVE Core - Anatomy and Physiology

Hemoglobin

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2024

Hemoglobin is a globular protein made up of four subunits. Two of these subunits are alpha chains, and the other two are beta chains. Each subunit contains a molecule of heme, which has an iron atom and can bind to oxygen. When an oxygen molecule binds to one heme group, it changes the shape of hemoglobin, making it easier for the other heme groups to bind oxygen as well. When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...

Staphylococcus aureus Growth using Human Hemoglobin as an Iron Source

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Cited by 31 •

2013

Here we describe a growth assay for Staphylococcus aureus using hemoglobin as the sole source of available nutrient iron. This assay establishes the role of bacterial factors involved in hemoglobin-derived iron acquisition.

A Rapid and Chemical-free Hemoglobin Assay with Photothermal Angular Light Scattering

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Cited by 1 •

2016

A photo-thermal angular light scattering (PT-AS) sensor enables the rapid and chemical-free hemoglobin assay of nanoliter-scale blood samples. Here, details of the PT-AS setup and a measurement protocol for the hemoglobin concentration in blood are provided. Representative results for anemic blood samples are also presented.

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